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A5GPX7 (PDXA_SYNR3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxythreonine-4-phosphate dehydrogenase

EC=1.1.1.262
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase
Gene names
Name:pdxA
Ordered Locus Names:SynRCC307_0033
OrganismSynechococcus sp. (strain RCC307) [Complete proteome] [HAMAP]
Taxonomic identifier316278 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NAD(P)-dependent oxidation of 4-(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP) By similarity. HAMAP-Rule MF_00536

Catalytic activity

4-phosphonooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH. HAMAP-Rule MF_00536

Cofactor

Binds 1 divalent metal cation per subunit By similarity.

Pathway

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. HAMAP-Rule MF_00536

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00536

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00536.

Miscellaneous

The active site is located at the dimer interface By similarity.

Sequence similarities

Belongs to the PdxA family.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpyridoxal phosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-hydroxythreonine-4-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

NAD binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3283284-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536
PRO_1000051523

Sites

Metal binding1601Divalent metal cation; shared with dimeric partner By similarity
Metal binding2031Divalent metal cation; shared with dimeric partner By similarity
Metal binding2691Divalent metal cation; shared with dimeric partner By similarity
Binding site1251Substrate By similarity
Binding site2771Substrate By similarity
Binding site2861Substrate By similarity
Binding site2951Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A5GPX7 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: DB8197D66D80824B

FASTA32835,324
        10         20         30         40         50         60 
MTRLAIALGD PAGIGAEVVL KALAHRPSLN PLLVGCRQWL QASYEQLLPC CHEPLADPSQ 

        70         80         90        100        110        120 
LEILDEPLTE AITPGSISAA AGAASFGWLT RATEAVLDGR AQALVTAPIA KTAWHQAGHH 

       130        140        150        160        170        180 
YPGQTERLAE LCGCDDAAML FTARSPQSGW RFNTLLATTH IPLSSVPAAL TPERLERRLG 

       190        200        210        220        230        240 
QLEDFCRRFR QRPRLRVAGL NPHAGEAGQL GTEEQRWITA CLQAYQQRHN NLQLEGPVPP 

       250        260        270        280        290        300 
DTCWLGAAQA WNDSQHVEEG CDGYLALYHD QGLIPVKVLA FDQAVNTTLG LPFLRTSPDH 

       310        320 
GTGFDRAGQG SARGASMLAA IDTAVELG 

« Hide

References

[1]Genoscope
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCC307.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CT978603 Genomic DNA. Translation: CAK26936.1.
RefSeqYP_001226289.1. NC_009482.1.

3D structure databases

ProteinModelPortalA5GPX7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316278.SynRCC307_0033.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK26936; CAK26936; SynRCC307_0033.
GeneID5156516.
KEGGsyr:SynRCC307_0033.
PATRIC23820910. VBISynSp108374_0033.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1995.
HOGENOMHOG000221591.
KOK00097.
OMAISIKLAM.
OrthoDBEOG6GN6ZC.

Enzyme and pathway databases

UniPathwayUPA00244; UER00312.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
HAMAPMF_00536. PdxA.
InterProIPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view]
PfamPF04166. PdxA. 1 hit.
[Graphical view]
TIGRFAMsTIGR00557. pdxA. 1 hit.
ProtoNetSearch...

Entry information

Entry namePDXA_SYNR3
AccessionPrimary (citable) accession number: A5GPX7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways